MolNFT v1 · #187503 · protein
Cryo-EM structure of human GPR158
7SHE: “Cryo-EM structure of human GPR158”. Electron microscopy, 3 ligands (CLR, PEE, EIJ). MolNFT v1 #187503 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7SHE
- Type
- protein
- Length
- 1,081 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5T848
- Ligands
- CLR, PEE, EIJ
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 541 | — | Q5T848 |
| B | — | protein | 540 | — | Q5T848 |
Ligands and binding sites
- CLR · Cholesterol · ligand · 22 copies · chains A, B
- PEE · 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine · ligand · chains A, B
- EIJ · (2S)-1-{[(S)-hydroxy{[(1s,2r,3r,4r,5s,6s)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}-3-(octadecanoyloxy)propan-2-yl (5E,8E,11E,14E)-icosa-5, 8,11,14-tetraenoate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q5T848
- Elsewhere: RCSB PDB 7SHE · PDBe 7SHE · UniProt Q5T848
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